BMRB Entry 27596

Name: 1H, 13C, 15N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1
Published: 2019-01-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27596

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, 15N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1

Deposition date:

2018-09-04

Original release date:

2019-01-10

Authors:

Bhattiprolu, Krishna; Gubens k, Nina; Wagner, Gabriel; Zechner, Ellen; Raffl, Sandra; Becker, Walter; Schrank, Evelyne; Zangger, Klaus

Citation:

Citation: Krishna, Bhattiprolu; Gubensak, Nina; Wagner, Gabriel; Zechner, Ellen; Raffl, Sandra; Becker, Walter; Schrank, Evelyne; Zangger, Klaus. "1H, 13C, 15N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1" Biomol. NMR Assignments 13, 121-125 (2019).
PubMed: 30617945

Assembly members:

Assembly members:
R1TraIC126, polymer, 127 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET Z2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
R1TraIC126: MNSVQPGAGNGEPVTAEVLA QRQAEEAIRRETERRADEIV RKMAENKPDLPDGKTELAVR DIAGQERDRSAISERETALP ESVLRESQREREAVREVARE NLLQERLQQMERDMVRDLQK EKTLGGD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	487
15N chemical shifts	119
1H chemical shifts	647

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	R1 Relaxosome	1

Entities:

Entity 1, R1 Relaxosome 127 residues - Formula weight is not available

Residues 2 - 127 corresponds to residues 1630 - 1756 Methionine 1 (M1) is added during the cloning.

1

MET

ASN

SER

VAL

GLN

PRO

GLY

ALA

GLY

ASN

2

GLY

GLU

PRO

VAL

THR

ALA

GLU

VAL

LEU

ALA

3

GLN

ARG

GLN

ALA

GLU

ALA

ILE

ARG

4

GLU

THR

GLU

ARG

ALA

ASP

GLU

ILE

VAL

5

ARG

LYS

MET

ALA

GLU

ASN

LYS

PRO

ASP

LEU

6

PRO

ASP

GLY

LYS

THR

GLU

LEU

ALA

VAL

ARG

7

ASP

ILE

ALA

GLY

GLN

GLU

ARG

ASP

ARG

SER

8

ALA

ILE

SER

GLU

ARG

GLU

THR

ALA

LEU

PRO

9

GLU

SER

VAL

LEU

ARG

GLU

SER

GLN

ARG

GLU

10

ARG

GLU

ALA

VAL

ARG

GLU

VAL

ALA

ARG

GLU

11

ASN

LEU

GLN

GLU

ARG

LEU

GLN

MET

12

GLU

ARG

ASP

MET

VAL

ARG

ASP

LEU

GLN

LYS

13

GLU

LYS

THR

LEU

GLY

ASP

Samples:

sample_1: R1TraIC126, [U-100% 15N], 300 uM; Na2HPO4 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks